The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Structural assembly of cullin-RING ubiquitin ligase complexes
Open accessAbstract
The cullin-RING ubiquitin ligases (CRLs) are the largest family of multi-subunit E3 ligases in eukaryotes, which ubiquitinate protein substrates in numerous cellular pathways. CRLs share a common arched scaffold and a RING domain catalytic subunit, but use different adaptors and substrate receptors to assemble unique E3 machineries. In comparison to the first CRL structure, recent findings have revealed increased complexity in the overall architecture and assembly mode of CRLs, including multi-domain organization, inter-domain flexibility, and subunit dimerization. These features highlight the capacity of CRLs to catalyze protein ubiquitination under distinct cellular contexts and in response to diverse signals. As the first installment of a two-review series, this article will focus on recent advances in our understanding of CRL assembly mechanisms.
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“Structural studies show that cul4 can rotate up to 150° around DDB1, the cRBN adaptor, generating a large ubiquitylation zone spacious enough to allow cRBN autoubiquitylation without a substrate being present (Zimmerman et al. 2010;Fischer et al. 2014).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Zimmerman et al. 2010
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“cDK12 therefore acts as a pseudo-substrate receptor which positions cycK within the expansive ubiquitylation zone of cRl4 ligases (Zimmerman et al. 2010;Słabicki et al. 2020a).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Zimmerman et al. 2010
Experimental — accuracy not yet measuredIn the citing paper
“ubiquitin E3 ligases serve as scaffolds between a target protein and an activated ubiquitin E2 conjugating enzyme charged with a ubiquitin molecule (E2–Ub), by binding both molecules, then catalysing the transfer of ubiquitin from the active site cysteine of the E2 onto a lysine side chain of a target protein104–107.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [104]
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Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224
Function and regulation of cullin–RING ubiquitin ligases
Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
Self-citationZhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480
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RetractedCarrillo, M. (2011) · California State University ScholarWorks (system-wide DSpace)
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Wang, Y., Yan, S., Yu, B., Gan, Y., Lei, J., Chen, C., Zhu, Z., Qiu, Z., & Cao, B. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.03.471130
Bosselut, R. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717970757.793469183
Zheng, N. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736847231.793569035
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Copeland, R. A. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733651684.793549798
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Liu, M., Wang, Y., Teng, F., Mai, X., Wang, X., Su, M.-Y., & Stjepanović, G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.04.519012
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Righetto, G. L., Yin, Y., Vu, V., Duda, D. M., Szewczyk, M. M., Zeng, H., Li, Y., Loppnau, P., Mei, T., Li, Y.-Y., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.15.553295
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Wang, W., Dai, Z., Liang, L., Mao, Y., & Yin, Y. (2025) · BioEssays · doi:10.1002/bies.202400175
Mistry, B. V., Alaiya, A. A., Abu‐Dawud, R., Al‐Yacoub, N., Çolak, D., Rajab, M., Alanazi, M., Shinwari, Z., Ahmed, H. A., Alharbi, T., et al. (2025) · Systems Biology in Reproductive Medicine · doi:10.1080/19396368.2025.2504459
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Wang, K., Kenny, S., Chagan, Z., Li, L., Das, C., & Liu, X. (2026) · Structure · doi:10.1016/j.str.2026.02.015
Regulation of proteotoxicity through atypical NEDDylation
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Martin, M. M. (2021) · theses.fr (ABES) · doi:10.70675/eba7934fzf9faz4427zb0f8zfba715ee98c9
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Larrous, P. (2023) · theses.fr (ABES) · doi:10.70675/fc16267dzad68z4beczb28bz9a828aba2035
Shen, M., Zhang, H., Chen, M., Yang, J., Yuchi, Z., 张华巍, & Liu, L. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117502
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Lee, R. M., Kim, K. P., & Joo, J. H. (2026) · The Journal of Microbiology · doi:10.71150/jm.2604001
Huber, F., Bernardinelli, E., Haddad, B. G., Klaus, S., Weitgasser, L., Roesch, S., Jakab, M., Konrat, R., Machtens, J., Eladari, D., et al. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-026-01283-6 · Cited by 1
BindingDB Entry 50016433: NAE modulators: A potential therapy for gastric carcinoma.
BindingDB (2023) · UC San Diego · doi:10.7270/q21c21wj
BindingDB (2024) · UC San Diego · doi:10.7270/q2vq374f
Metadata
- Authors
- Zimmerman, E. S., Schulman, B. A., & Zheng, N.
- Affiliations
- University of Washington (US)
- St. Jude Children's Research Hospital (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Zheng, Ning
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 20
- Issue
- 6
- Pages
- 714-721
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC3070871
- OpenAlex
- W2029890158
- Cited by
- 227
- References
- 62
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 12 · 2023: 11 · 2022: 14 · 2021: 14 · 2020: 15 · 2019: 18 · 2018: 13 · 2017: 12 · 2016: 17 · 2015: 18 · 2014: 14 · 2013: 21 · 2012: 17
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (R01CA107134)
- National Institute of General Medical Sciences (F32GM093497, R01GM069530)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- cullin-RING ubiquitin ligases, E3 ubiquitin ligase, ubiquitination, RING domain, adaptor proteins, substrate receptor, subunit dimerization
- MeSH terms
- Animals, Humans, Protein Structure, Secondary, Protein Structure, Quaternary, Ubiquitin-Protein Ligases, F-Box Proteins, Protein Multimerization
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